3vgc: Difference between revisions
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|PDB= 3vgc |SIZE=350|CAPTION= <scene name='initialview01'>3vgc</scene>, resolution 1.67Å | |PDB= 3vgc |SIZE=350|CAPTION= <scene name='initialview01'>3vgc</scene>, resolution 1.67Å | ||
|SITE= <scene name='pdbsite=CAT:The+Catalytic+Site+Which+Includes+The+Modified+SER+That+...'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:The+Catalytic+Site+Which+Includes+The+Modified+SER+That+...'>CAT</scene> | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SRB:L-1-NAPHTHYL-2-ACETAMIDO-ETHANE+BORONIC+ACID'>SRB</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vgc OCA], [http://www.ebi.ac.uk/pdbsum/3vgc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3vgc RCSB]</span> | |||
}} | }} | ||
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[[Category: Pai, E F.]] | [[Category: Pai, E F.]] | ||
[[Category: Stoll, V S.]] | [[Category: Stoll, V S.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:36:35 2008'' | ||
Revision as of 05:36, 31 March 2008
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| , resolution 1.67Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Chymotrypsin, with EC number 3.4.21.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GAMMA-CHYMOTRYPSIN L-NAPHTHYL-1-ACETAMIDO BORONIC ACID ACID INHIBITOR COMPLEX
OverviewOverview
In order to probe the structural basis of stereoselectivity in the serine protease family, a series of enantiomeric boronic acids RCH2CH(NHCOCH3)B(OH)2 has been synthesized and kinetically characterized as transition-state analog inhibitors using alpha-chymotrypsin and subtilisin Carlsberg as model systems. When the R-substituent in this series was changed from a p-chlorophenyl to a 1-naphthyl group, alpha-chymotrypsin, but not subtilisin, reversed its usual preference for l-enantiomers and bound more tightly to the D-enantiomer [Martichonok, V., & Jones, J. B. (1996) J. Am. Chem. Soc. 118, 950-958]. The structural factors responsible for the differences in stereoselectivity between the two enzymes have been explored by X-ray crystallographic examination of subtilisin Carlsberg and gamma-chymotrypsin complexes of the L- and D-enantiomers of p-chlorophenyl and 1-naphthyl boronic acid derivatives. In both enzymes, the L-isomers of the inhibitors, which are more closely related to the natural L-amino acid substrates, form tetrahedral adducts, covalently linking the central boron atom and Ogamma of the catalytic serine. The d-isomers, however, differ in the way they interact with subtilisin or gamma-chymotrypsin. With subtilisin, both the D-p-chlorophenyl and D-1-naphthyl inhibitor complexes form covalent Ser Ogamma-to-boron bonds, but with gamma-chymotrypsin, the same inhibitors lead to novel tetrahedral adducts covalently linking both Ser195 Ogamma and His57 Nepsilon2 covalently via the boron atom.
About this StructureAbout this Structure
3VGC is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes., Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF, Biochemistry. 1998 Jan 13;37(2):451-62. PMID:9425066
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